Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution
about
Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzymeMolecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironmentNMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand bindingMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesTotal conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzymeChanges in protein structure at the interface accompanying complex formation.TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix.Tissue inhibitors of matrix metalloproteinases in cancer.The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityLow resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein.The anti-angiogenic peptide, loop 6, binds insulin-like growth factor-1 receptor.Dynamic interdomain interactions contribute to the inhibition of matrix metalloproteinases by tissue inhibitors of metalloproteinases.Epigenetic regulation of matrix metalloproteinases and their collagen substrates in cancer.Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.An integrin-binding N-terminal peptide region of TIMP-2 retains potent angio-inhibitory and anti-tumorigenic activity in vivo.Growth-stimulatory activity of TIMP-2 is mediated through c-Src activation followed by activation of FAK, PI3-kinase/AKT, and ERK1/2 independent of MMP inhibition in lung adenocarcinoma cellsTissue inhibitors of metalloproteinases in cell signaling: metalloproteinase-independent biological activities.Tissue inhibitor of metalloproteinases-4. The road less traveled.Engineered Tissue Inhibitor of Metalloproteinases-3 Variants Resistant to Endocytosis Have Prolonged Chondroprotective Activity.A peptide derived from TIMP-3 inhibits multiple angiogenic growth factor receptors and tumour growth and inflammatory arthritis in mice.Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix.Tissue inhibitor of metalloproteinases (TIMPs) in heart failure.Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: a new frontier in TIMP engineering.Endostatin binds to the catalytic domain of matrix metalloproteinase-2.Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme.Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase.Delineating the molecular basis of the inactivity of tissue inhibitor of metalloproteinase-2 against tumor necrosis factor-alpha-converting enzyme.Characterization of an Atypical Metalloproteinase Inhibitors Like Protein (Sbp8-1) From Scallop Byssus.Matrix metalloproteinase (MMP-2, -9) and tissue inhibitor (TIMP-1, -2) activity in tear samples of pediatric type 1 diabetic patients
P2860
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P2860
Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@ast
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@en
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@nl
type
label
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@ast
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@en
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@nl
prefLabel
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@ast
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@en
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@nl
P2093
P50
P3181
P356
P1476
Three-dimensional structure of ...... teinases-2 at 2.1 A resolution
@en
P2093
Bergmann U
Fernandez-Catalan C
Tryggvason K
Tuuttila A
P304
P3181
P356
10.1006/JMBI.1998.2223
P407
P577
1998-12-01T00:00:00Z